scholarly article | Q13442814 |
P50 | author | Thomas Huber | Q40143826 |
Gottfried Otting | Q21994180 | ||
Aaron J. Oakley | Q37377804 | ||
Moeava Tehei | Q38802506 | ||
Nicholas E. Dixon | Q54252257 | ||
Andrew Robinson | Q64682054 | ||
P2093 | author name string | Nan Li | |
Hiromasa Yagi | |||
Slobodan Jergic | |||
Kiyoshi Ozawa | |||
Karin V Loscha | |||
Zhi-Qiang Xu | |||
Flynn R Hill | |||
Nicholas P Horan | |||
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The C-terminal domain of dnaQ contains the polymerase binding site | Q33991949 | ||
In vivo photocrosslinking with unnatural amino Acid mutagenesis | Q34156648 | ||
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The proofreading exonuclease subunit epsilon of Escherichia coli DNA polymerase III is tethered to the polymerase subunit alpha via a flexible linker | Q36859313 | ||
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Lanthanide labeling offers fast NMR approach to 3D structure determinations of protein-protein complexes. | Q54468874 | ||
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A bipartite polymerase-processivity factor interaction: only the internal beta binding site of the alpha subunit is required for processive replication by the DNA polymerase III holoenzyme. | Q54485462 | ||
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In vivo assembly of overproduced DNA polymerase III. Overproduction, purification, and characterization of the alpha, alpha-epsilon, and alpha-epsilon-theta subunits | Q71246230 | ||
The structure of T. aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases | Q80228429 | ||
Phage like it HOT: solution structure of the bacteriophage P1-encoded HOT protein, a homolog of the theta subunit of E. coli DNA polymerase III | Q81088334 | ||
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P275 | copyright license | Creative Commons Attribution-NonCommercial 3.0 Unported | Q18810331 |
P6216 | copyright status | copyrighted | Q50423863 |
P433 | issue | 10 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Escherichia coli | Q25419 |
P304 | page(s) | 5354-5367 | |
P577 | publication date | 2013-04-10 | |
P1433 | published in | Nucleic Acids Research | Q135122 |
P1476 | title | Proofreading exonuclease on a tether: the complex between the E. coli DNA polymerase III subunits α, epsilon, θ and β reveals a highly flexible arrangement of the proofreading domain | |
P478 | volume | 41 |